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Folate receptor gamma (FR-gamma) (Folate receptor 3)

 FOLR3_HUMAN             Reviewed;         243 AA.
P41439; J3KQ90; Q05C14;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-OCT-2017, entry version 127.
RecName: Full=Folate receptor gamma;
Short=FR-gamma;
AltName: Full=Folate receptor 3;
Flags: Precursor;
Name=FOLR3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Hematopoietic;
PubMed=8110752; DOI=10.1021/bi00171a021;
Shen F., Ross J.F., Wang X., Ratnam M.;
"Identification of a novel folate receptor, a truncated receptor, and
receptor type beta in hematopoietic cells: cDNA cloning, expression,
immunoreactivity, and tissue specificity.";
Biochemistry 33:1209-1215(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-204 (ISOFORM 3).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
CHARACTERIZATION.
PubMed=7727426; DOI=10.1021/bi00016a042;
Shen F., Wu M., Ross J.F., Miller D., Ratnam M.;
"Folate receptor type gamma is primarily a secretory protein due to
lack of an efficient signal for glycosylphosphatidylinositol
modification: protein characterization and cell type specificity.";
Biochemistry 34:5660-5665(1995).
[5]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
-!- FUNCTION: Binds to folate and reduced folic acid derivatives and
mediates delivery of 5-methyltetrahydrofolate to the interior of
cells. Isoform Short does not bind folate.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Long;
IsoId=P41439-1; Sequence=Displayed;
Name=Short;
IsoId=P41439-2; Sequence=VSP_001506;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3;
IsoId=P41439-3; Sequence=VSP_055089;
Note=No experimental confirmation available. Ref.3 (AAH30285)
sequence is in conflict in position: 76:E->V. {ECO:0000305};
-!- TISSUE SPECIFICITY: Spleen, thymus, bone marrow, ovarian
carcinoma, and uterine carcinoma.
-!- SIMILARITY: Belongs to the folate receptor family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH30285.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Z32564; CAA83553.1; -; mRNA.
EMBL; Z32633; CAA83566.1; -; mRNA.
EMBL; U08471; AAA18382.1; -; mRNA.
EMBL; U08470; AAA18381.1; -; mRNA.
EMBL; AP000812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030285; AAH30285.1; ALT_INIT; mRNA.
PIR; A53506; A53506.
RefSeq; NP_000795.2; NM_000804.3.
RefSeq; NP_001304974.1; NM_001318045.1.
UniGene; Hs.352; -.
ProteinModelPortal; P41439; -.
SMR; P41439; -.
BioGrid; 108635; 1.
DrugBank; DB05168; EC145.
DrugBank; DB00158; Folic Acid.
iPTMnet; P41439; -.
PhosphoSitePlus; P41439; -.
BioMuta; FOLR3; -.
DMDM; 1169723; -.
MaxQB; P41439; -.
PeptideAtlas; P41439; -.
PRIDE; P41439; -.
DNASU; 2352; -.
Ensembl; ENST00000442948; ENSP00000411161; ENSG00000110203. [P41439-2]
GeneID; 2352; -.
KEGG; hsa:2352; -.
UCSC; uc058ezu.1; human. [P41439-1]
CTD; 2352; -.
DisGeNET; 2352; -.
EuPathDB; HostDB:ENSG00000110203.8; -.
GeneCards; FOLR3; -.
H-InvDB; HIX0035971; -.
HGNC; HGNC:3795; FOLR3.
MIM; 602469; gene.
neXtProt; NX_P41439; -.
OpenTargets; ENSG00000110203; -.
PharmGKB; PA28211; -.
GeneTree; ENSGT00390000010470; -.
HOGENOM; HOG000006539; -.
HOVERGEN; HBG039612; -.
InParanoid; P41439; -.
KO; K13649; -.
PhylomeDB; P41439; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
GenomeRNAi; 2352; -.
PRO; PR:P41439; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110203; -.
CleanEx; HS_FOLR3; -.
ExpressionAtlas; P41439; baseline and differential.
Genevisible; P41439; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0019898; C:extrinsic component of membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0005542; F:folic acid binding; TAS:ProtInc.
GO; GO:0015884; P:folic acid transport; TAS:ProtInc.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
InterPro; IPR004269; Folate_rcpt.
InterPro; IPR018143; Folate_rcpt-like.
InterPro; IPR032934; FR-gamma.
PANTHER; PTHR10517; PTHR10517; 1.
PANTHER; PTHR10517:SF17; PTHR10517:SF17; 1.
Pfam; PF03024; Folate_rec; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond;
Folate-binding; Glycoprotein; Receptor; Reference proteome; Secreted;
Signal.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 243 Folate receptor gamma.
/FTId=PRO_0000008810.
REGION 122 126 Folate binding.
{ECO:0000250|UniProtKB:P15328}.
REGION 155 160 Folate binding.
{ECO:0000250|UniProtKB:P15328}.
BINDING 101 101 Folate. {ECO:0000250|UniProtKB:P15328}.
BINDING 105 105 Folate. {ECO:0000250|UniProtKB:P15328}.
BINDING 194 194 Folate. {ECO:0000250|UniProtKB:P15328}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 63 {ECO:0000250|UniProtKB:P15328}.
DISULFID 55 103 {ECO:0000250|UniProtKB:P15328}.
DISULFID 64 107 {ECO:0000250|UniProtKB:P15328}.
DISULFID 87 173 {ECO:0000250|UniProtKB:P15328}.
DISULFID 94 144 {ECO:0000250|UniProtKB:P15328}.
DISULFID 133 207 {ECO:0000250|UniProtKB:P15328}.
DISULFID 137 187 {ECO:0000250|UniProtKB:P15328}.
DISULFID 150 167 {ECO:0000250|UniProtKB:P15328}.
VAR_SEQ 55 105 CSPWKKNACCTASTSQELHKDTSRLYNFNWDHCGKMEPTCK
RHFIQDSCLY -> VGAPQGPSPGSVPLDDLPGAEEPEYGG
DGCGGERLSPVSSPPSAVPGRRMPAARPAPARSCTRTPPAC
TTLTGITVVRWNPPASATLSRTAVS (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055089.
VAR_SEQ 105 243 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_001506.
CONFLICT 43 43 T -> I (in Ref. 3; AAH30285).
{ECO:0000305}.
SEQUENCE 243 AA; 27638 MW; AC7636EB5355647B CRC64;
MAWQMMQLLL LALVTAAGSA QPRSARARTD LLNVCMNAKH HKTQPSPEDE LYGQCSPWKK
NACCTASTSQ ELHKDTSRLY NFNWDHCGKM EPTCKRHFIQ DSCLYECSPN LGPWIRQVNQ
SWRKERILNV PLCKEDCERW WEDCRTSYTC KSNWHKGWNW TSGINECPAG ALCSTFESYF
PTPAALCEGL WSHSFKVSNY SRGSGRCIQM WFDSAQGNPN EEVAKFYAAA MNAGAPSRGI
IDS


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